Reference : The CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
The CphAII protein from Aquifex aeolicus exhibits a metal-dependent phosphodiesterase activity
Kupper, Michaël [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > > > >]
Bauvois, Cédric [Institut de recherches microbiologiques J.M. Wiame > Cristallographie des Protéines > > >]
Frère, Jean-Marie [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Galleni, Moreno [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Bebrone, Carine mailto [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > > > >]
Extremophiles: Life Under Extreme Conditions
Springer Science & Business Media B.V.
Yes (verified by ORBi)
[en] The CphAII protein from the hyperthermophile Aquifex aeolicus shows the five conserved motifs of the metallo-β-lactamase (MBL) superfamily and presents 28% identity with the Aeromonas hydrophila subclass B2 CphA MBL. The gene encoding CphAII was amplified by PCR from the A. aeolicus genomic DNA and overexpressed in Escherichia coli using a pLex-based expression system. The recombinant CphAII protein was purified by a combination of heating (to denature E. coli proteins) and two steps of immobilized metal affinity chromatography. The purified enzyme preparation did not exhibit a β-lactamase activity but showed a metal-dependent phosphodiesterase activity versus bis-p-nitrophenyl phosphate and thymidine 5'-monophosphate p-nitrophenyl ester, with an optimum at 85°C. The circular dichroism spectrum was in agreement with the percentage of secondary structures characteristic of the MBL αββα fold.
Politique Scientifique Fédérale (Belgique) = Belgian Federal Science Policy ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
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